Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD)
Serum transferrin (Tf) is the essential iron transport protein in the body. Transferrin is responsible for the sequestration of free iron in serum and the delivery of iron throughout the body and into cells, where iron is released inside a mildly acidified endosome. Altered iron distributions are as...
Gespeichert in:
Veröffentlicht in: | Free radical biology & medicine 2021-06, Vol.169, p.416-424 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 424 |
---|---|
container_issue | |
container_start_page | 416 |
container_title | Free radical biology & medicine |
container_volume | 169 |
creator | Tubbesing, Kate Khoo, Ting Chean Bahreini Jangjoo, Shahab Sharikova, Anna Barroso, Margarida Khmaladze, Alexander |
description | Serum transferrin (Tf) is the essential iron transport protein in the body. Transferrin is responsible for the sequestration of free iron in serum and the delivery of iron throughout the body and into cells, where iron is released inside a mildly acidified endosome. Altered iron distributions are associated with diseases such as iron-overload, cancer, and cardiovascular disease. The presence of free iron is linked to deleterious redox reactions, inside and outside cells and organelles. As Tf iron release is pH dependent, any changes in intraorganelle and extracellular pH, often associated with disease progression, could inhibit normal iron delivery or accelerate iron release in the wrong compartment. However, imaging approaches to monitor changes in the iron-bound state of Tf are lacking. Recently, Raman spectroscopy has been shown to measure iron-bound forms of Tf in solution, intact cells and tissue samples. Here, a biochemical Raman assay has been developed to identify iron-release from Tf following modification of chemical environment. Quantitative singular value decomposition (SVD) method has been applied to discriminate between iron-bound Tf samples during endocytic trafficking in intact cancer cells subjected to Raman hyperspectral confocal imaging. We demonstrate the strength of the SVD method to monitor pH-induced Tf iron-release using Raman hyperspectral imaging, providing the redox biology field with a novel tool that facilitates subcellular investigation of the iron-binding profile of transferrin in various disease models.
[Display omitted]
•Raman spectroscopy differentiates iron-bound and iron-free transferrin (Tf),key for investigating iron transport regulation.•Raman hyperspectral imaging can evaluate pH-induced Tf iron release in the endocytic compartments of intact, unlabeled cells.•Singular value decomposition enables complex Raman data analysis by semi-automated unbiased discrimination of Tf iron-binding profiles. |
doi_str_mv | 10.1016/j.freeradbiomed.2021.04.030 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_33930515</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0891584921002768</els_id><sourcerecordid>2520869773</sourcerecordid><originalsourceid>FETCH-LOGICAL-c491t-484a532112d8268e117c09c1d7735a972d75524ad600026059144b933de3210c3</originalsourceid><addsrcrecordid>eNqNkV2L1DAYhYso7rj6FyTgzYq05rNNEQQZV11YEPy6DWnydjZDJ6lJO7J3_nRTZxzcu71KIM85Oe97iuIFwRXBpH69rfoIELXtXNiBrSimpMK8wgw_KFZENqzkoq0fFissW1IKyduz4klKW4wxF0w-Ls4YaxkWRKyK31cx-LJz3jq_QQaGYR50RGMMvRsAhR5NUfvUQ4zOozkt1KA7GMolBPqid9qjm9sRYhrBZHZAbqc3C6a9RQv_13CvhxmQBRN2Y0hucsGji68_3r98Wjzq9ZDg2fE8L75_uPy2_lRef_54tX53XRrekqnkkmvBKCHUSlpLIKQxuDXENg0Tum2obYSgXNs6T0lrLFrCedcyZiGrsGHnxduD7zh3eWsG_BJWjTHHjbcqaKfuvnh3ozZhr2RdNxjLbHBxNIjh5wxpUjuXloVpD2FOigqKZd3mPBl9c0BNDClF6E_fEKyWDtVW3elQLR0qzFXuMKuf_5_0pP1XWgbkAfgFXeiTceANnLA8fy0YJpLmGxZrN-ll2-sw-ylLX91fmunLAw25mL2DqI4K62IuW9ng7jXRH5M_16M</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2520869773</pqid></control><display><type>article</type><title>Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD)</title><source>MEDLINE</source><source>Web of Science - Science Citation Index Expanded - 2021<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" /></source><source>Access via ScienceDirect (Elsevier)</source><creator>Tubbesing, Kate ; Khoo, Ting Chean ; Bahreini Jangjoo, Shahab ; Sharikova, Anna ; Barroso, Margarida ; Khmaladze, Alexander</creator><creatorcontrib>Tubbesing, Kate ; Khoo, Ting Chean ; Bahreini Jangjoo, Shahab ; Sharikova, Anna ; Barroso, Margarida ; Khmaladze, Alexander</creatorcontrib><description>Serum transferrin (Tf) is the essential iron transport protein in the body. Transferrin is responsible for the sequestration of free iron in serum and the delivery of iron throughout the body and into cells, where iron is released inside a mildly acidified endosome. Altered iron distributions are associated with diseases such as iron-overload, cancer, and cardiovascular disease. The presence of free iron is linked to deleterious redox reactions, inside and outside cells and organelles. As Tf iron release is pH dependent, any changes in intraorganelle and extracellular pH, often associated with disease progression, could inhibit normal iron delivery or accelerate iron release in the wrong compartment. However, imaging approaches to monitor changes in the iron-bound state of Tf are lacking. Recently, Raman spectroscopy has been shown to measure iron-bound forms of Tf in solution, intact cells and tissue samples. Here, a biochemical Raman assay has been developed to identify iron-release from Tf following modification of chemical environment. Quantitative singular value decomposition (SVD) method has been applied to discriminate between iron-bound Tf samples during endocytic trafficking in intact cancer cells subjected to Raman hyperspectral confocal imaging. We demonstrate the strength of the SVD method to monitor pH-induced Tf iron-release using Raman hyperspectral imaging, providing the redox biology field with a novel tool that facilitates subcellular investigation of the iron-binding profile of transferrin in various disease models.
[Display omitted]
•Raman spectroscopy differentiates iron-bound and iron-free transferrin (Tf),key for investigating iron transport regulation.•Raman hyperspectral imaging can evaluate pH-induced Tf iron release in the endocytic compartments of intact, unlabeled cells.•Singular value decomposition enables complex Raman data analysis by semi-automated unbiased discrimination of Tf iron-binding profiles.</description><identifier>ISSN: 0891-5849</identifier><identifier>EISSN: 1873-4596</identifier><identifier>DOI: 10.1016/j.freeradbiomed.2021.04.030</identifier><identifier>PMID: 33930515</identifier><language>eng</language><publisher>NEW YORK: Elsevier Inc</publisher><subject>Biochemistry & Molecular Biology ; Cancer ; Endocrinology & Metabolism ; Endosomes - metabolism ; Hyperspectral Imaging ; Iron ; Iron - metabolism ; Life Sciences & Biomedicine ; Raman hyperspectral imaging ; Receptors, Transferrin ; Redox biology ; Science & Technology ; Transferrin</subject><ispartof>Free radical biology & medicine, 2021-06, Vol.169, p.416-424</ispartof><rights>2021 Elsevier Inc.</rights><rights>Copyright © 2021 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>8</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000653018200005</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c491t-484a532112d8268e117c09c1d7735a972d75524ad600026059144b933de3210c3</citedby><cites>FETCH-LOGICAL-c491t-484a532112d8268e117c09c1d7735a972d75524ad600026059144b933de3210c3</cites><orcidid>0000-0003-0330-3595 ; 0000-0002-7054-3524 ; 0000-0001-7646-9970 ; 0000-0002-0407-3181 ; 0000-0001-6418-7984 ; 0000-0002-0451-4653</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.freeradbiomed.2021.04.030$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,315,782,786,887,3552,27931,27932,39265,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33930515$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tubbesing, Kate</creatorcontrib><creatorcontrib>Khoo, Ting Chean</creatorcontrib><creatorcontrib>Bahreini Jangjoo, Shahab</creatorcontrib><creatorcontrib>Sharikova, Anna</creatorcontrib><creatorcontrib>Barroso, Margarida</creatorcontrib><creatorcontrib>Khmaladze, Alexander</creatorcontrib><title>Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD)</title><title>Free radical biology & medicine</title><addtitle>FREE RADICAL BIO MED</addtitle><addtitle>Free Radic Biol Med</addtitle><description>Serum transferrin (Tf) is the essential iron transport protein in the body. Transferrin is responsible for the sequestration of free iron in serum and the delivery of iron throughout the body and into cells, where iron is released inside a mildly acidified endosome. Altered iron distributions are associated with diseases such as iron-overload, cancer, and cardiovascular disease. The presence of free iron is linked to deleterious redox reactions, inside and outside cells and organelles. As Tf iron release is pH dependent, any changes in intraorganelle and extracellular pH, often associated with disease progression, could inhibit normal iron delivery or accelerate iron release in the wrong compartment. However, imaging approaches to monitor changes in the iron-bound state of Tf are lacking. Recently, Raman spectroscopy has been shown to measure iron-bound forms of Tf in solution, intact cells and tissue samples. Here, a biochemical Raman assay has been developed to identify iron-release from Tf following modification of chemical environment. Quantitative singular value decomposition (SVD) method has been applied to discriminate between iron-bound Tf samples during endocytic trafficking in intact cancer cells subjected to Raman hyperspectral confocal imaging. We demonstrate the strength of the SVD method to monitor pH-induced Tf iron-release using Raman hyperspectral imaging, providing the redox biology field with a novel tool that facilitates subcellular investigation of the iron-binding profile of transferrin in various disease models.
[Display omitted]
•Raman spectroscopy differentiates iron-bound and iron-free transferrin (Tf),key for investigating iron transport regulation.•Raman hyperspectral imaging can evaluate pH-induced Tf iron release in the endocytic compartments of intact, unlabeled cells.•Singular value decomposition enables complex Raman data analysis by semi-automated unbiased discrimination of Tf iron-binding profiles.</description><subject>Biochemistry & Molecular Biology</subject><subject>Cancer</subject><subject>Endocrinology & Metabolism</subject><subject>Endosomes - metabolism</subject><subject>Hyperspectral Imaging</subject><subject>Iron</subject><subject>Iron - metabolism</subject><subject>Life Sciences & Biomedicine</subject><subject>Raman hyperspectral imaging</subject><subject>Receptors, Transferrin</subject><subject>Redox biology</subject><subject>Science & Technology</subject><subject>Transferrin</subject><issn>0891-5849</issn><issn>1873-4596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>EIF</sourceid><recordid>eNqNkV2L1DAYhYso7rj6FyTgzYq05rNNEQQZV11YEPy6DWnydjZDJ6lJO7J3_nRTZxzcu71KIM85Oe97iuIFwRXBpH69rfoIELXtXNiBrSimpMK8wgw_KFZENqzkoq0fFissW1IKyduz4klKW4wxF0w-Ls4YaxkWRKyK31cx-LJz3jq_QQaGYR50RGMMvRsAhR5NUfvUQ4zOozkt1KA7GMolBPqid9qjm9sRYhrBZHZAbqc3C6a9RQv_13CvhxmQBRN2Y0hucsGji68_3r98Wjzq9ZDg2fE8L75_uPy2_lRef_54tX53XRrekqnkkmvBKCHUSlpLIKQxuDXENg0Tum2obYSgXNs6T0lrLFrCedcyZiGrsGHnxduD7zh3eWsG_BJWjTHHjbcqaKfuvnh3ozZhr2RdNxjLbHBxNIjh5wxpUjuXloVpD2FOigqKZd3mPBl9c0BNDClF6E_fEKyWDtVW3elQLR0qzFXuMKuf_5_0pP1XWgbkAfgFXeiTceANnLA8fy0YJpLmGxZrN-ll2-sw-ylLX91fmunLAw25mL2DqI4K62IuW9ng7jXRH5M_16M</recordid><startdate>20210601</startdate><enddate>20210601</enddate><creator>Tubbesing, Kate</creator><creator>Khoo, Ting Chean</creator><creator>Bahreini Jangjoo, Shahab</creator><creator>Sharikova, Anna</creator><creator>Barroso, Margarida</creator><creator>Khmaladze, Alexander</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0330-3595</orcidid><orcidid>https://orcid.org/0000-0002-7054-3524</orcidid><orcidid>https://orcid.org/0000-0001-7646-9970</orcidid><orcidid>https://orcid.org/0000-0002-0407-3181</orcidid><orcidid>https://orcid.org/0000-0001-6418-7984</orcidid><orcidid>https://orcid.org/0000-0002-0451-4653</orcidid></search><sort><creationdate>20210601</creationdate><title>Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD)</title><author>Tubbesing, Kate ; Khoo, Ting Chean ; Bahreini Jangjoo, Shahab ; Sharikova, Anna ; Barroso, Margarida ; Khmaladze, Alexander</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-484a532112d8268e117c09c1d7735a972d75524ad600026059144b933de3210c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Biochemistry & Molecular Biology</topic><topic>Cancer</topic><topic>Endocrinology & Metabolism</topic><topic>Endosomes - metabolism</topic><topic>Hyperspectral Imaging</topic><topic>Iron</topic><topic>Iron - metabolism</topic><topic>Life Sciences & Biomedicine</topic><topic>Raman hyperspectral imaging</topic><topic>Receptors, Transferrin</topic><topic>Redox biology</topic><topic>Science & Technology</topic><topic>Transferrin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tubbesing, Kate</creatorcontrib><creatorcontrib>Khoo, Ting Chean</creatorcontrib><creatorcontrib>Bahreini Jangjoo, Shahab</creatorcontrib><creatorcontrib>Sharikova, Anna</creatorcontrib><creatorcontrib>Barroso, Margarida</creatorcontrib><creatorcontrib>Khmaladze, Alexander</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Free radical biology & medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tubbesing, Kate</au><au>Khoo, Ting Chean</au><au>Bahreini Jangjoo, Shahab</au><au>Sharikova, Anna</au><au>Barroso, Margarida</au><au>Khmaladze, Alexander</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD)</atitle><jtitle>Free radical biology & medicine</jtitle><stitle>FREE RADICAL BIO MED</stitle><addtitle>Free Radic Biol Med</addtitle><date>2021-06-01</date><risdate>2021</risdate><volume>169</volume><spage>416</spage><epage>424</epage><pages>416-424</pages><issn>0891-5849</issn><eissn>1873-4596</eissn><abstract>Serum transferrin (Tf) is the essential iron transport protein in the body. Transferrin is responsible for the sequestration of free iron in serum and the delivery of iron throughout the body and into cells, where iron is released inside a mildly acidified endosome. Altered iron distributions are associated with diseases such as iron-overload, cancer, and cardiovascular disease. The presence of free iron is linked to deleterious redox reactions, inside and outside cells and organelles. As Tf iron release is pH dependent, any changes in intraorganelle and extracellular pH, often associated with disease progression, could inhibit normal iron delivery or accelerate iron release in the wrong compartment. However, imaging approaches to monitor changes in the iron-bound state of Tf are lacking. Recently, Raman spectroscopy has been shown to measure iron-bound forms of Tf in solution, intact cells and tissue samples. Here, a biochemical Raman assay has been developed to identify iron-release from Tf following modification of chemical environment. Quantitative singular value decomposition (SVD) method has been applied to discriminate between iron-bound Tf samples during endocytic trafficking in intact cancer cells subjected to Raman hyperspectral confocal imaging. We demonstrate the strength of the SVD method to monitor pH-induced Tf iron-release using Raman hyperspectral imaging, providing the redox biology field with a novel tool that facilitates subcellular investigation of the iron-binding profile of transferrin in various disease models.
[Display omitted]
•Raman spectroscopy differentiates iron-bound and iron-free transferrin (Tf),key for investigating iron transport regulation.•Raman hyperspectral imaging can evaluate pH-induced Tf iron release in the endocytic compartments of intact, unlabeled cells.•Singular value decomposition enables complex Raman data analysis by semi-automated unbiased discrimination of Tf iron-binding profiles.</abstract><cop>NEW YORK</cop><pub>Elsevier Inc</pub><pmid>33930515</pmid><doi>10.1016/j.freeradbiomed.2021.04.030</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-0330-3595</orcidid><orcidid>https://orcid.org/0000-0002-7054-3524</orcidid><orcidid>https://orcid.org/0000-0001-7646-9970</orcidid><orcidid>https://orcid.org/0000-0002-0407-3181</orcidid><orcidid>https://orcid.org/0000-0001-6418-7984</orcidid><orcidid>https://orcid.org/0000-0002-0451-4653</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0891-5849 |
ispartof | Free radical biology & medicine, 2021-06, Vol.169, p.416-424 |
issn | 0891-5849 1873-4596 |
language | eng |
recordid | cdi_pubmed_primary_33930515 |
source | MEDLINE; Web of Science - Science Citation Index Expanded - 2021<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; Access via ScienceDirect (Elsevier) |
subjects | Biochemistry & Molecular Biology Cancer Endocrinology & Metabolism Endosomes - metabolism Hyperspectral Imaging Iron Iron - metabolism Life Sciences & Biomedicine Raman hyperspectral imaging Receptors, Transferrin Redox biology Science & Technology Transferrin |
title | Iron-binding cellular profile of transferrin using label-free Raman hyperspectral imaging and singular value decomposition (SVD) |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T18%3A33%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Iron-binding%20cellular%20profile%20of%20transferrin%20using%20label-free%20Raman%20hyperspectral%20imaging%20and%20singular%20value%20decomposition%20(SVD)&rft.jtitle=Free%20radical%20biology%20&%20medicine&rft.au=Tubbesing,%20Kate&rft.date=2021-06-01&rft.volume=169&rft.spage=416&rft.epage=424&rft.pages=416-424&rft.issn=0891-5849&rft.eissn=1873-4596&rft_id=info:doi/10.1016/j.freeradbiomed.2021.04.030&rft_dat=%3Cproquest_pubme%3E2520869773%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2520869773&rft_id=info:pmid/33930515&rft_els_id=S0891584921002768&rfr_iscdi=true |